Comparison of the amide proton exchange behavior of the rapidly formed folding intermediate and the native state of an antibody scFv fragment
Open Access
- 21 April 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 407 (1) , 42-46
- https://doi.org/10.1016/s0014-5793(97)00306-2
Abstract
We have investigated the stability of backbone amide protons of the intermediate and the native state of the scFv fragment of an antibody. Stopped flow experiments analyzed by MS and NMR detected the...Keywords
This publication has 34 references indexed in Scilit:
- Folding Nuclei of the scFv Fragment of an AntibodyBiochemistry, 1996
- Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR StudyBiochemistry, 1995
- A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein FoldingJournal of Molecular Biology, 1995
- Amide Hydrogen Exchange in a Highly Denatured State: Hen Egg-white Lysozyme in UreaJournal of Molecular Biology, 1994
- Detection of Transient Protein Folding Populations by Mass SpectrometryScience, 1993
- Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopyBiochemistry, 1993
- Characterization of the linker peptide of the single‐chain Fv fragment of an antibody by NMR spectroscopyFEBS Letters, 1993
- Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMRBiochemistry, 1992
- Phosphocholine binding immunoglobulin Fab McPC603Journal of Molecular Biology, 1986
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983